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Proteomics News - January 2012 Archives
Researchers have identified a new and unusual role for a key player in the human immune system. A protein initially believed to regulate one routine function within the cell has proven vital for another critical step in the activation of the immune system.
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 | Using computer models and laboratory experiments, scientists from Rice University and the University of California, San Diego have probed the structure of the protein mitoNEET to better understand its role in aging, cancer and diabetes. They found the protein could untangle its arms at one end to loosen its grip on a potentially toxic molecule of iron and sulfur. Their research is described this week in the Proceedings of the National Academy of Sciences. ...> Full Article |
Berkeley Lab scientists are reporting the first 3-D images of an individual protein ever obtained with enough clarity to determine its structure.
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 | A special group of proteins, the so-called chaperons, helps other proteins to obtain their correct conformation. Until now scientists supposed that hydrolyzing ATP provides the energy for the large conformational changes of chaperon Hsp90. Now a research team from the Nanosystems Initiative Munich could prove that Hsp90 utilizes thermal fluctuations as the driving force for its conformational changes. The renowned journal PNAS reports on their findings. ...> Full Article |
 | Using a blend of technologies, scientists from the Florida campus of the Scripps Research Institute have painted a new picture of how biochemical information can be transmitted through the modification of a protein. Previously, scientists believed that during the pairing of proteins and their binding partners ("ligands"), proteins modified their shape while ligands remained stable. The new study shows this one-size-fits-all solution is not entirely accurate.
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The binding of proteins to substrates is essential for organic life. In the 54th issue of Science China, one paper investigates the relationship between environmental temperature and the capture radius for protein binding. It was found that the largest capture radius corresponds to the folding transition temperature of a protein chain. The results could provide valuable reference data for future research.
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Sequence comparisons are an essential tool for the prediction and analysis of the structure and functions of proteins. A new method developed by computational biologists at the LMU permits sequence comparisons to be performed faster and more accurately than ever before.
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